Yellow fever virus cDNA and Antigen

Yellow fever is a mosquito-borne tropical disease caused by the yellow fever virus. Symptoms can include fever, jaundice, muscle pain, nausea, vomiting and fatigue. In rare cases, it can progress to a more severe form, which can cause bleeding and organ failure. Vaccination is the best way to prevent yellow fever.

The specific antigens used to detect yellow fever virus infection are the nucleoprotein (NP) and envelope (E) proteins. Antibodies to the NP and E proteins can be detected using immunoassays such as ELISA (enzyme-linked immunosorbent assay), Western blot, and immunofluorescence.

The Yellow Fever Virus genome is composed of single-stranded, positive-sense RNA. It is about 10.7 kilobases in length and encodes three structural proteins and seven non-structural proteins. The structural proteins are the capsid protein, envelope protein, and the membrane protein. The non-structural proteins are the enzymes required for viral replication, transcription, and translation.

One of the key proteins of YFV is the envelope protein (E), which is responsible for the attachment of the virus to host cells and the fusion of the viral and cellular membranes. Another important protein is the small envelope protein M, which plays a role in the assembly and release of the virus particles. The protein C is involved in the maturation of the virus particle, and non-structural protein 1 and 2A are important for viral replication.

Serine protease subunit NS2B is an essential component of the YFV replication complex, which processes the viral polyprotein into its functional components. The non-structural protein 2A-alpha is also involved in the processing of the viral polyprotein and plays a role in the suppression of host immune responses.

The study of these proteins and their interactions with host cells is crucial for developing antiviral therapies and vaccines against YFV. Several drugs that target YFV proteins are currently under investigation, including those that inhibit the protease activity of NS2B/NS3 and those that target the fusion activity of the envelope protein.

In conclusion, the proteins of YFV play critical roles in the virus life cycle and pathogenesis. Understanding the functions of these proteins and their interactions with host cells is essential for the development of effective treatments and vaccines against this deadly virus.

The use of recombinant proteins/cDNA in academic research and therapeutic applications has skyrocketed. However, in heterologous expression systems, successful recombinant protein expression is dependent on a variety of factors, including codon preference, RNA secondary structure, and GC content. When compared to pre-optimization, more and more experimental results demonstrated that the expression level was dramatically increased, ranging from two to hundred times depending on the gene. Bioclone has created a proprietary technology platform that has resulted in the creation of over 6,000 artificially synthesized codon-optimized cDNA clones (cloned in E. coli expression Vector), which are ready for production of the recombinant proteins.